The NER protein Rad33 shows functional homology to human Centrin2 and is involved in modification of Rad4

Dulk, Ben den; Eijk, Patrick van; Ruijter, M de; Brandsma, Jourica A.; Brouwer, Jaap

doi:10.1016/j.dnarep.2008.02.004

Cited by 24 publications

(16 citation statements)

References 62 publications

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“…6A). However, we did reproduce the result by den Dulk et al [39] that the rad33Δ mutant shows a reduction (2-fold in our experiment) in Rad4 levels (Fig. 6A).…”

Section: Resultssupporting

confidence: 88%

“…4, 7A). A previous report on Rad4 has shown that several unidentified modified forms of Rad4 increase in UV-treated rad33Δ cells compared to wt [39]. Based on this report and our finding that Rad4 was sumoylated, we asked if levels of Rad4 sumoylation would be altered in rad33Δ .…”

Section: Resultsmentioning

confidence: 83%

“…Another mechanism for how Rad4 sumoylation might be controlled was suggested by den Dulk et al [39], who showed that an unidentified UV-induced modification was increased in the rad33Δ mutant and also in a rad4 mutant that disrupted the interaction between Rad4 and Rad33. Assuming that this modification is SUMO, one interpretation of this result would be that the interaction with Rad33 inhibits Rad4 sumoylation.…”

Section: Discussionmentioning

confidence: 99%

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A role for SUMO in nucleotide excision repair

et al. 2011

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The two Siz/PIAS SUMO E3 ligases Siz1 and Siz2 are responsible for the vast majority of sumoylation in Saccharomyces cerevisiae. We found that siz1Δ siz2Δ mutants are sensitive to UV light. Epistasis analysis showed that the SIZ genes act in the nucleotide excision repair (NER) pathway, and suggested that they participate both in global genome repair (GGR) and in the Rpb9-dependent subpathway of transcription-coupled repair (TCR), but have minimal role in Rad26-dependent TCR. Quantitative analysis of NER at the single-nucleotide level showed that siz1Δ siz2Δ is deficient in repair of both the transcribed and non-transcribed strands of the DNA. These experiments confirmed that the SIZ genes participate in GGR. Their role in TCR remains unclear. It has been reported previously that mutants deficient for the SUMO conjugating enzyme Ubc9 contain reduced levels of Rad4, the yeast homolog of human XPC. However, our experiments do not support the conclusion that SUMO conjugation affects Rad4 levels. We found that several factors that participate in NER are sumoylated, including Rad4, Rad16, Rad7, Rad1, Rad10, Ssl2, Rad3, and Rpb4. Although Rad16 was heavily sumoylated, elimination of the major SUMO attachment sites in Rad16 had no detectable effect on UV resistance or removal of DNA lesions. SUMO attachment to most of these NER factors was significantly increased by DNA damage. Furthermore, SUMO-modified Rad4 accumulated in NER mutants that block the pathway downstream of Rad4, suggesting that SUMO becomes attached to Rad4 at a specific point during its functional cycle. Collectively, these results suggest that SIZ-dependent sumoylation may modulate the activity of multiple proteins to promote efficient NER.

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“…6A). However, we did reproduce the result by den Dulk et al [39] that the rad33Δ mutant shows a reduction (2-fold in our experiment) in Rad4 levels (Fig. 6A).…”

Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 83%

Section: Discussionmentioning

confidence: 99%

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A role for SUMO in nucleotide excision repair

et al. 2011

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“…The TAP tag consists of a calmodulin binding peptide (CBP), a tobacco etch virus protease (TEV protease) cleavage site, and two IgG binding domains of protein A (25). The Rad4TAP strain has been used previously to study Rad4 modification and degradation, and the tagged protein proved to be as functional as the unmodified Rad4 (29). Indeed, our UV survival data also indicate that Rad4TAP is fully functional in NER (supplemental Fig.…”

Section: Cells Lacking Ubp3 Activity Are More Resistant To Uvmentioning

confidence: 65%

Yeast Deubiquitinase Ubp3 Interacts with the 26 S Proteasome to Facilitate Rad4 Degradation

Mao

Smerdon

2010

Journal of Biological Chemistry

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Deubiquitinating enzymes (DUBs) function in a variety of cellular processes by removing ubiquitin moieties from substrates, but their role in DNA repair has not been elucidated. Yeast Rad4-Rad23 heterodimer is responsible for recognizing DNA damage in nucleotide excision repair (NER). Rad4 binds to UV damage directly while Rad23 stabilizes Rad4 from proteasomal degradation. Here, we show that disruption of yeast deubiquitinase UBP3 leads to enhanced UV resistance, increased repair of UV damage and Rad4 levels in rad23⌬ cells, and elevated Rad4 stability. A catalytically inactive Ubp3 (Ubp3-C469A), however, is unable to affect NER or Rad4. Consistent with its role in downregulating Rad4, Ubp3 physically interacts with Rad4 and the proteasome, both in vivo and in vitro, suggesting that Ubp3 associates with the proteasome to facilitate Rad4 degradation and thus suppresses NER.

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“…Cetn2-null DT40 cells displayed no defects in centrosome formation or cell division but were reported to be hypersensitive to UV irradiation [15]. The nuclear excision repair protein Rad33 appears functionally homologous to Cetn2 [18]. The centrin-associated protein pericentrin (PCNT) (OMIM: 605925) has also been implicated in DNA damage repair [96].…”

Section: Centrins and Pericentrinmentioning

confidence: 99%

Nuclear roles for cilia-associated proteins

McClure-Begley

Klymkowsky

2017

Cilia

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Cilia appear to be derived, evolutionarily, from structures present in the ancestral (pre-ciliary) eukaryote, such as microtubule-based vesicle trafficking and chromosome segregation systems. Experimental observations suggest that the ciliary gate, the molecular complex that mediates the selective molecular movement between cytoplasmic and ciliary compartments, shares features with nuclear pores. Our hypothesis is that this shared transport machinery is at least partially responsible for the observation that a number of ciliary and ciliogenesis-associated proteins are found within nuclei where they play roles in the regulation of gene expression, DNA repair, and nuclear import and export. Recognizing the potential for such nuclear roles is critical when considering the phenotypic effects that arise from the mutational modification of ciliary proteins.Electronic supplementary materialThe online version of this article (doi:10.1186/s13630-017-0052-x) contains supplementary material, which is available to authorized users.

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The NER protein Rad33 shows functional homology to human Centrin2 and is involved in modification of Rad4

Cited by 24 publications

References 62 publications

A role for SUMO in nucleotide excision repair

A role for SUMO in nucleotide excision repair

Yeast Deubiquitinase Ubp3 Interacts with the 26 S Proteasome to Facilitate Rad4 Degradation

Nuclear roles for cilia-associated proteins

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